ID HIS2_BURTA Reviewed; 122 AA. AC Q2SUB0; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 16-JUN-2009, entry version 26. DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisE; OrderedLocusNames=BTH_I2985; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., RA Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., RA Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., RA Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., RA Roberts K., Hatch B., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-ATP + H(2)O = 1-(5- CC phosphoribosyl)-AMP + diphosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the PRA-PH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000086; ABC38054.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_443489.2; -. DR GeneID; 3849842; -. DR GenomeReviews; CP000086_GR; BTH_I2985. DR KEGG; bte:BTH_I2985; -. DR TIGR; BTH_I2985; -. DR HOGENOM; Q2SUB0; -. DR BioCyc; BTHA271848:BTH_I2985-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01020; -; 1. DR InterPro; IPR008179; PRib-ATP_pyrophosphohydrolase. DR Pfam; PF01503; PRA-PH; 1. DR ProDom; PD002611; Pra_PH/CH; 1. DR TIGRFAMs; TIGR03188; histidine_hisI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Nucleotide-binding. FT CHAIN 1 122 Phosphoribosyl-ATP pyrophosphatase. FT /FTId=PRO_0000319643. SQ SEQUENCE 122 AA; 13369 MW; AE30624E57BA9D27 CRC64; MTQPTIEDTL LRLAAVIDSR KGGDPEQSYV SRLFHKGDDA VLKKIGEEAT EVVLAAKDVR QGGAPSALVG EVADLWFHCL VALSHFDLSP ADVIAELERR EGMSGIEEKA LRKRREREEN GG //